C
Christophe Braet
Researcher at Ghent University
Publications - 4
Citations - 174
Christophe Braet is an academic researcher from Ghent University. The author has contributed to research in topics: Trichoderma reesei & Cellobiose. The author has an hindex of 4, co-authored 4 publications receiving 172 citations.
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Journal ArticleDOI
Engineering of a glycosidase Family 7 cellobiohydrolase to more alkaline pH optimum: the pH behaviour of Trichoderma reesei Cel7A and its E223S/ A224H/L225V/T226A/D262G mutant.
D. Becker,Christophe Braet,Harry Brumer,Marc Claeyssens,Christina Divne,B. R. Fagerstrom,Mark Harris,T.A. Jones,Gerard J. Kleywegt,Anu Koivula,Sabah Mahdi,Katheleen Piens,Michael L. Sinnott,Jerry Ståhlberg,Tuula T. Teeri,M. Underwood,Gerd Wohlfahrt +16 more
TL;DR: X-ray crystallography of the catalytic domain of the E223S/A224H/L225V/T226A/D262G mutant reveals that major differences from the wild-type are confined to the mutations themselves, and inhibition by cellobiose is certainly relieved in the mutant.
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A novel thermostable α-galactosidase from the thermophilic fungus Thermomyces lanuginosus CBS 395.62/b: Purification and characterization
Judit M. Rezessy-Szabó,Quang D. Nguyen,Ágoston Hoschke,Christophe Braet,Gyöngyi Hajós,Marc Claeyssens +5 more
TL;DR: Amo acid sequence alignment of N-terminal sequence data allows the α-galactosidase from Thermomyces lanuginosus to be classified in glycosyl hydrolase family 36.
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Inhibition of cellobiohydrolases from Trichoderma reesei. Synthesis and evaluation of some glucose-, cellobiose-, and cellotriose-derived hydroximolactams and imidazoles.
Stefan Vonhoff,Kathleen Piens,Muriel Pipelier,Christophe Braet,Marc Claeyssens,Andrea Vasella +5 more
TL;DR: The results strongly suggest that shape requirements must be met by glycosidase inhibitors before they can be used to characterize the proton trajectory of Glycosidases.
Journal ArticleDOI
Glycosylated Rat Prolactin: Isolation and Structural Characterization
TL;DR: In vitro, glycosylation of rat prolactin modulates immune recognition through steric hindrance of the access to the epitope sites and HPAE-PAD analysis identified NeuAc subtypes.